Search Results - "Tishkov, V I"

Catalytic mechanism and application of formate dehydrogenase by Tishkov, V. I., Popov, V. O.

“…NAD super(+)-dependent formate dehydrogenase (FDH) is an abundant enzyme that plays an important role in energysupply of methylotrophic microorganisms and in…”
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Horseradish peroxidase: Modulation of properties by chemical modification of protein and heme by Zakharova, G. S., Uporov, I. V., Tishkov, V. I.

“…Horseradish peroxidase (HRP) is one of the most studied enzymes of the plant peroxidase superfamily. HRP is also widely used in different bioanalytical…”
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Improvement of the soy formate dehydrogenase properties by rational design by Kargov, I.S., Kleimenov, S.Y., Savin, S.S., Tishkov, V.I., Alekseeva, A.A.

“…Previous experiments on substitution of the residue Phe290 to Asp, Asn and Ser in NAD+-dependent formate dehydrogenase from soya Glycine max (SoyFDH) showed…”
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Engineering of substrate specificity of D-amino acid oxidase from the yeast Trigonopsis variabilis: Directed mutagenesis of Phe258 residue by Komarova, N. V., Golubev, I. V., Khoronenkova, S. V., Chubar’, T. A., Tishkov, V. I.

“…Natural D-amino acid oxidases (DAAO) are not suitable for selective determination of D-amino acids due to their broad substrate specificity profiles. Analysis…”
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D-Amino acid oxidase: Physiological role and applications by Khoronenkova, S. V, Tishkov, V. I

“…D-Amino acids play a key role in regulation of many processes in living cells. FAD-dependent D-amino acid oxidase (DAAO) is one of the most important enzymes…”
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Additivity of the Stabilization Effect of Single Amino Acid Substitutions in Triple Mutants of Recombinant Formate Dehydrogenase from the Soybean Glycine max by Alekseeva, A A, Kargov, I S, Kleimenov, S Yu, Savin, S S, Tishkov, V I

“…Recently, we demonstrated that the amino acid substitutions Ala267Met and Ala267Met/Ile272Val (Alekseeva et al., Biochemistry, 2012), Phe290Asp, Phe290Asn and…”
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Development of an approach to determining enzymatic activity of ribonucleoside hydrolase c using hydrophilic interaction liquid chromatography by Shaposhnikov, L.A., Chikurova, N.Yu, Chernobrovkina, A.V., Tishkov, V.I., Pometun, A.A.

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Formate Dehydrogenase: From NAD(P)H Regeneration to Targeting Pathogen Biofilms, Composing Highly Efficient Hybrid Biocatalysts and Atmospheric CO2 Fixation by Tishkov, V. I., Pometun, A. A., Savin, S. S.

“…NAD(P) + -dependent formate dehydrogenase (EC 1.2.1.2, FDH) catalyzes the simplest reaction from chemical and biological points of view, oxidation of…”
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The role of Tyr102 residue in the functioning of bacterial NAD+-dependent formate dehydrogenase of Pseudomonas sp. 101 by Popinako, А.V., Pometun, А.А., Nilov, D.K., Dibrova, D.V., Khrustalev, V.V., Khrustaleva, T.A., Iurchenko, T.S., Nikolaeva, А.Yu, Švedas, V.K., Boyko, K.М., Tishkov, V.I., Popov, V.О.

“…Once you have missed the first button …, you'll never manage to button up Johann Wolfgang von Goethe Formate oxidation is a final step of methanol oxidation in…”
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Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and Crystallization by Pometun, A. A., Boyko, K. M., Yurchenko, T. S., Nikolaeva, A. Yu, Kargov, I. S., Atroshenko, D. L., Savin, S. S., Popov, V. O., Tishkov, V. I.

“…NAD + -dependent formate dehydrogenase from Staphylococcus aureus (SauFDH) is one of the key enzymes responsible for the survival of this pathogen in the form…”
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Effect of His6-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fusca by Parshin, P. D., Pometun, A. A., Martysuk, U. A., Kleymenov, S. Yu, Atroshenko, D. L., Pometun, E. V., Savin, S. S., Tishkov, V. I.

“…Phenylacetone monooxygenase (EC 1.14.13.92, PAMO) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters. PAMO is a…”
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Physiological Role of D-amino Acids and Bioanalytical Potential of D-amino Acid Oxidases by Tishkov, V. I., Shelomov, M. D., Pometun, A. A., Savin, S. S., Atroshenko, D. L.

“…D-amino acid oxidase (DAAO) plays an important role in the functioning of both prokaryotes and eukaryotes. DAAO is increasingly being used in practice,…”
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High Throughput Screening in Drug Discovery: Problems and Solutions by Hushpulian, D. M., Gaisina, I. N., Nikulin, S. V., Chubar, T. A., Savin, S. S., Gazaryan, I. G., Tishkov, V. I.

“…World-wide introduction of high throughput screening (HTS) methods in drug discovery research did not result in the increased number of novel medications on…”
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Engineering the N-Terminal Sequence of Glycine max Soybean Formate Dehydrogenase by Shaposhnikov, L. A., Savin, S. S., Atroshenko, D. L., Chubar, T. A., Pometun, E. V., Tishkov, V. I., Pometun, A. A.

“…NAD(P) + -dependent formate dehydrogenase (FDH, EC 1.2.1.2.) catalyzes the oxidation of formate ion with the coupled reduction of NAD(P) + to NAD(P)H…”
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Effect of the Components of a Buffer Solution on the Catalytic Activity of the NAD+-Dependent Formate Dehydrogenase from the Bacterium Staphylococcus aureus by Iurchenko, T. S., Bolotova, S. B., Loginova, A. A., Pometun, E. V., Savin, S. S., Pometun, A. A., Tishkov, V. I.

“…NAD + -dependent formate dehydrogenase (FDH, EC 1.2.1.2) from bacterium Staphylococcus aureus (SauFDH) is the most active enzyme among FDHs of this group;…”
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Highly Stable Mutant Bacterial Formate Dehydrogenase with Improved Catalytic Properties by Pometun, A. A., Shirokova, A. A., Galanicheva, N. P., Shaposhnikov, L. A., Atroshenko, D. L., Pometun, E. V., Tishkov, V. I., Savin, S. S.

“…NAD + -dependent formate dehydrogenase (FDH, EC 1.2.1.2) from methylotrophic bacterium Pseudomonas sp.101 (PseFDH) has one of the highest thermal stability…”
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Role of a Structurally Equivalent Phenylalanine Residue in Catalysis and Thermal Stability of Formate Dehydrogenases from Different Sources by Tishkov, V. I., Goncharenko, K. V., Alekseeva, A. A., Kleymenov, S. Yu, Savin, S. S.

“…Comparison of amino acid sequences of NAD + -dependent formate dehydrogenases (FDH, EC 1.2.1.2) from different sources and analysis of structures of holo-forms…”
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Kinetics of Thermoinactivation of D-Amino Acid Oxidase OPADAAO1 from the Ogataea parapolymorpha DL-1 Yeast by Koshkina, M. K., Sergeyev, E. P., Fedorov, T. A., Shelomov, M. D., Pometun, A. A., Savin, S. S., Tishkov, V. I., Atroshenko, D. L.

“…Our earlier annotation of the genome of the yeast Ogataea parapolymorpha DL-1 made it possible to identify five genes of potential D-amino acids oxidases. All…”
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Structure-activity relationship for branched oxyquinoline HIF activators: Effect of modifications to phenylacetamide “tail” by Poloznikov, A.A., Zakhariants, A.A., Nikulin, S.V., Smirnova, N.A., Hushpulian, D.M., Gaisina, I.N., Tonevitsky, A.G., Tishkov, V.I., Gazaryan, I.G.

“…HIF prolyl hydroxylase is a major regulator of HIF stability. Branched tail oxyquinolines have been identified as specific inhibitors of HIF prolyl hydroxylase…”
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A comparative study of the thermal stability of formate dehydrogenases from microorganisms and plants by Sadykhov, E G, Serov, A E, Voinova, N S, Uglanova, S V, Petrov, A S, Alekseeva, A A, Kleimenov, SYu, Popov, VO, Tishkov, VI

“…A comparative study of the thermostability of NAD^sup +^-dependent formate dehydrogenases (FDHs; EC 1.2.1.2) from both methylotrophic bacteria Pseudomonas sp…”
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